Author

D. P. Hoogerheide

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:host-pathogen & immune response· 2 Approach:biophysical modeling· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Organism:virus· 1

Frequent Co-Authors

P. A. Gurnev· 2 shared S. M. Bezrukov· 2 shared T. K. Rostovtseva· 2 shared A. Lai· 1 shared A. Laszlo· 1 shared A. Rovini· 1 shared D. Jacobs· 1 shared E. E. Heldwein· 1 shared

Activity by Year

2021-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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2 shared papersBiophysics

P. A. Gurnev

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Author profile →

3 papers

Recent·Most cited

Restricting α-Synuclein Transport into Mitochondria by Inhibition of α-Synuclein-VDAC Complexation as a Potential Therapeutic Target for Parkinson's Disease Treatment

M. Rajendran, M. Queralt-Martin, P. A. Gurnev, W. M. Rosencrans, A. Rovini, D. Jacobs, K. Abrantes, D. P. Hoogerheide, S. M. Bezrukov, T. K. Rostovtseva

This study shows that a peptide from hexokinase 2 inhibits alpha-synuclein-VDAC complexation, reducing alpha-synuclein mitochondrial translocation and toxicity in Parkinson's disease.

bioRxiv · Apr 7, 2022Biophysics

MspA Porin as a Local Nanopore Probe for Membrane-bound Proteins

D. P. Hoogerheide, P. A. Gurnev, J. Gundlach, A. Laszlo, T. K. Rostovtseva, S. M. Bezrukov

The paper demonstrates that the M2MspA nanopore can replace VDAC for studying Synuclein interactions, preserving key features of nanopore-based protein detection.

bioRxiv · Oct 15, 2021 · PreprintBiophysics

Highly basic clusters in the HSV-1 nuclear egress complex drive membrane budding by inducing lipid ordering

M. K. Thorsen, A. Lai, M. W. Lee, D. P. Hoogerheide, G. C. L. Wong, J. H. Freed, E. E. Heldwein

This study identifies how basic regions in the HSV-1 nuclear egress complex induce lipid ordering and negative curvature to drive membrane budding, with phosphorylation inhibiting this process.

bioRxiv · May 18, 2021Microbiology